Isolation and recovery of biologically active proteins is currently very difficult. Current solutions rely on energy intensive methods such as evaporative/diffusive, electrophoresis and porous tube adhesion. These methods are utilized to remove undesired ions or compounds from solutions. One example of such a method is reverse osmosis. In some instances, no methodologies exist to remove the undesired ion or compound.
Current systems for recovering biologically active protein for treatment of autoimmune deficiencies, AIDS, Hemophilia Lupus and the like are inadequate due to low yield, the requirements for labor-intensive operations, and costs. Specific examples of these 20-50 nm length −50,000 Dalton proteins are interferon, insulin, and clotting factor VIII. Current methods such as porous tube adhesion use ultra-filtration to isolate and then manually harvest the proteins. Unfortunately, tube thickness impedes flow of solvent plasmas and disrupts the protein's integrity resulting in low yield of the process.
Most biologically active proteins are ionically charged at their extremities. The proteins are moderately soluble in water and remain polar in that condition. Many disease-treating proteins are harvested from living tissue or in bulk in Vitro solutions. These include low animal plasma slurries including, but not limited to interferon (human and selected hominid), insulin (bovine and synthetic hominid), and cascade clotting factor VIII for hemophilia. Current methods rely on capillary action to “stall” the desired protein at a specific location and invoke subsequent action (such as rinsing and/or diffusion), to gradually recover the isolated protein of interest. The resulting protein removal frequently traumatizes and de-natures the protein. Rinsing must “rip” the protein from the many-thousand nanometer deep porosity surface on which it is held. Typical permeates (the output of the harvester) must be further centrifuged to deliver pharmaceutical grade reagents. Current sequestration membranes and porous tubes are believed to be quite thick and therefore their thickness ratio is less flow efficient.
Therefore, there is a need in the art for sequestration membranes, which are much thinner but still allow for efficient collection of proteins. Moreover, there is a need in the art for a device that separates proteins without damaging the protein during the collection and removal process.